Cofilin 1

Last updated
CFL1
Protein CFL1 PDB 1q8g.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases CFL1 , CFL, HEL-S-15, cofilin, cofilin 1
External IDs OMIM: 601442 MGI: 101757 HomoloGene: 99735 GeneCards: CFL1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005507

NM_007687

RefSeq (protein)

NP_005498

NP_031713

Location (UCSC) Chr 11: 65.82 – 65.86 Mb Chr 19: 5.54 – 5.55 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Cofilin 1 (non-muscle; n-cofilin), also known as CFL1, is a human gene, part of the ADF/cofilin family.

Contents

Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus. [5]

One group reports that reelin signaling leads to serine3-phosphorylation of cofilin-1, and this interaction may play a role in the reelin-related regulation of neuronal migration. [6] [7]

Interactions

Cofilin 1 has been shown to interact with HSPH1 [8] and LIMK1. [9] [10]

Related Research Articles

<span class="mw-page-title-main">ADF/Cofilin family</span>

ADF/cofilin is a family of actin-binding proteins associated with the rapid depolymerization of actin microfilaments that give actin its characteristic dynamic instability. This dynamic instability is central to actin's role in muscle contraction, cell motility and transcription regulation.

<span class="mw-page-title-main">Myosin light-chain kinase</span> Class of kinase enzymes

Myosin light-chain kinase also known as MYLK or MLCK is a serine/threonine-specific protein kinase that phosphorylates a specific myosin light chain, namely, the regulatory light chain of myosin II.

<span class="mw-page-title-main">LIM domain</span> InterPro Domain

LIM domains are protein structural domains, composed of two contiguous zinc fingers, separated by a two-amino acid residue hydrophobic linker. The domain name is an acronym of the three genes in which it was first identified. LIM is a protein interaction domain that is involved in binding to many structurally and functionally diverse partners. The LIM domain appeared in eukaryotes sometime prior to the most recent common ancestor of plants, fungi, amoeba and animals. In animal cells, LIM domain-containing proteins often shuttle between the cell nucleus where they can regulate gene expression, and the cytoplasm where they are usually associated with actin cytoskeletal structures involved in connecting cells together and to the surrounding matrix, such as stress fibers, focal adhesions and adherens junctions.

<span class="mw-page-title-main">ROCK1</span> Protein

ROCK1 is a protein serine/threonine kinase also known as rho-associated, coiled-coil-containing protein kinase 1. Other common names are ROKβ and P160ROCK. ROCK1 is a major downstream effector of the small GTPase RhoA and is a regulator of the actomyosin cytoskeleton which promotes contractile force generation. ROCK1 plays a role in cancer and in particular cell motility, metastasis, and angiogenesis.

<span class="mw-page-title-main">LIMK1</span> Protein-coding gene in the species Homo sapiens

LIM domain kinase 1 is an enzyme that in humans is encoded by the LIMK1 gene.

<span class="mw-page-title-main">Alpha-actinin-4</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.

<span class="mw-page-title-main">RAC2</span> Protein-coding gene in the species Homo sapiens

Rac2 is a small signaling G protein, and is a member of the Rac subfamily of the family Rho family of GTPases. It is encoded by the gene RAC2.

<span class="mw-page-title-main">RhoC</span> Protein-coding gene in the species Homo sapiens

RhoC is a small signaling G protein, and is a member of the Rac subfamily of the family Rho family of GTPases. It is encoded by the gene RHOC.

<span class="mw-page-title-main">LIMK2</span> Protein-coding gene in the species Homo sapiens

LIM domain kinase 2 is an enzyme that in humans is encoded by the LIMK2 gene.

<span class="mw-page-title-main">CDC42BPA</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein kinase MRCK alpha is an enzyme that in humans is encoded by the CDC42BPA gene.

<span class="mw-page-title-main">SSH1</span> Protein-coding gene in the species Homo sapiens

For the SSH-1 protocol, see Secure Shell#Version 1

<span class="mw-page-title-main">PSTPIP1</span> Enzyme found in humans

Proline-serine-threonine phosphatase-interacting protein 1 is an enzyme that in humans is encoded by the PSTPIP1 gene.

<span class="mw-page-title-main">DYRK1B</span> Protein-coding gene in the species Homo sapiens

Dual specificity tyrosine-phosphorylation-regulated kinase 1B is an enzyme that in humans is encoded by the DYRK1B gene.

<span class="mw-page-title-main">LASP1</span> Protein-coding gene in the species Homo sapiens

LIM and SH3 domain protein 1 is a protein that in humans is encoded by the LASP1 gene.

<span class="mw-page-title-main">SSH2</span> Protein-coding gene in the species Homo sapiens

Protein phosphatase Slingshot homolog 2 is an enzyme that in humans is encoded by the SSH2 gene.

<span class="mw-page-title-main">Stress fiber</span> Contractile actin bundles found in non-muscle cells

Stress fibers are contractile actin bundles found in non-muscle cells. They are composed of actin (microfilaments) and non-muscle myosin II (NMMII), and also contain various crosslinking proteins, such as α-actinin, to form a highly regulated actomyosin structure within non-muscle cells. Stress fibers have been shown to play an important role in cellular contractility, providing force for a number of functions such as cell adhesion, migration and morphogenesis.

<span class="mw-page-title-main">TESK1</span> Protein-coding gene in the species Homo sapiens

Dual specificity testis-specific protein kinase 1 is an enzyme that in humans is encoded by the TESK1 gene.

<span class="mw-page-title-main">SSH3</span> Protein-coding gene in the species Homo sapiens

Protein phosphatase Slingshot homolog 3 is an enzyme that in humans is encoded by the SSH3 gene.

<span class="mw-page-title-main">Cofilin-2</span> Protein found in humans

Cofilin 2 (muscle) also known as CFL2 is a protein which in humans is encoded by the CFL2 gene.

<span class="mw-page-title-main">Rho-associated protein kinase</span>

Rho-associated protein kinase (ROCK) is a kinase belonging to the AGC family of serine-threonine specific protein kinases. It is involved mainly in regulating the shape and movement of cells by acting on the cytoskeleton.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000172757 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000056201 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: CFL1 cofilin 1 (non-muscle)".
  6. Chai X, Förster E, Zhao S, Bock HH, Frotscher M (January 2009). "Reelin stabilizes the actin cytoskeleton of neuronal processes by inducing n-cofilin phosphorylation at serine3". J. Neurosci. 29 (1): 288–99. doi:10.1523/JNEUROSCI.2934-08.2009. PMC   6664910 . PMID   19129405.
  7. Frotscher M, Chai X, Bock HH, Haas CA, Förster E, Zhao S (April 2009). "Role of Reelin in the development and maintenance of cortical lamination". J Neural Transm . 116 (11): 1451–5. doi:10.1007/s00702-009-0228-7. PMID   19396394. S2CID   1310387.
  8. Saito Y, Doi K, Yamagishi N, Ishihara K, Hatayama T (Feb 2004). "Screening of Hsp105alpha-binding proteins using yeast and bacterial two-hybrid systems". Biochem. Biophys. Res. Commun. 314 (2): 396–402. doi:10.1016/j.bbrc.2003.12.108. PMID   14733918.
  9. Foletta VC, Lim MA, Soosairajah J, Kelly AP, Stanley EG, Shannon M, He W, Das S, Massague J, Bernard O, Soosairaiah J (Sep 2003). "Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1". J. Cell Biol. 162 (6): 1089–98. doi:10.1083/jcb.200212060. PMC   2172847 . PMID   12963706.
  10. Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S (Aug 1999). "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase". Science . 285 (5429): 895–8. doi:10.1126/science.285.5429.895. PMID   10436159.

Further reading